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Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Simian immunodeficiency virus agm.vervet (isolate AGM155) (SIV-agm.ver) (Simian immunodeficiency virus African green monkey vervet)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation (By similarity).By similarity
Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristointegration complex. The myristoylation signal and the NLS exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu (By similarity).By similarity
Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with host PPIA/CYPA protects the virus from restriction by host TRIM5-alpha and from an unknown antiviral activity in host cells. This capsid restriction by TRIM5 is one of the factors which restricts SIV to the simian species (By similarity).By similarity
Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity).By similarity
The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. Hydrolyzes host EIF4GI and PABP1 in order to shut off the capped cellular mRNA translation. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).PROSITE-ProRule annotation
Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H can probably proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).By similarity
Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the SIV genome, a 5 bp duplication of host DNA is produced at the ends of SIV integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity).By similarity

Miscellaneous

The 155 isolate is from a monkey imported from Kenya.
The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template switching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs.

Catalytic activityi

Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.PROSITE-ProRule annotation
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
  • Mg2+By similarityNote: Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding.By similarity
  • Mg2+By similarityNote: Magnesium ions are required for integrase activity. Binds at least 1, maybe 2 magnesium ions.By similarity

Enzyme regulationi

The viral protease is inhibited by many synthetic protease inhibitors (PIs), such as amprenavir, atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and saquinavir. RT can be inhibited either by nucleoside RT inhibitors (NRTIs) or by non nucleoside RT inhibitors (NNRTIs). NRTIs act as chain terminators, whereas NNRTIs inhibit DNA polymerization by binding a small hydrophobic pocket near the RT active site and inducing an allosteric change in this region. Classical NRTIs are abacavir, adefovir (PMEA), didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir (PMPA), zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs are atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266), emivirine (I-EBU), and nevirapine (BI-RG-587). The tritherapies used as a basic effective treatment of AIDS associate two NRTIs and one NNRTI. Use of protease inhibitors in tritherapy regimens permit more ambitious therapeutic strategies.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei229 – 230Cis/trans isomerization of proline peptide bond; by human PPIA/CYPABy similarity2
Active sitei536For protease activity; shared with dimeric partnerPROSITE-ProRule annotation1
Metal bindingi724Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi799Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi800Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Sitei1014Essential for RT p66/p51 heterodimerizationBy similarity1
Sitei1027Essential for RT p66/p51 heterodimerizationBy similarity1
Metal bindingi1056Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1091Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1111Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1162Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1237Magnesium; catalytic; for integrase activityBy similarity1
Metal bindingi1289Magnesium; catalytic; for integrase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri398 – 415CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri419 – 436CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1176 – 1217Integrase-typePROSITE-ProRule annotationAdd BLAST42
DNA bindingi1396 – 1443Integrase-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAspartyl protease, DNA-binding, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed DNA polymerase, Transferase, Viral nucleoprotein
Biological processDNA integration, DNA recombination, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Viral genome integration, Viral penetration into host nucleus, Viral release from host cell, Virion maturation, Virus entry into host cell
LigandMagnesium, Metal-binding, Zinc

Protein family/group databases

MEROPSiA02.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Gag-Pol polyprotein
Alternative name(s):
Pr160Gag-Pol
Cleaved into the following 9 chains:
Matrix protein p17
Short name:
MA
Capsid protein p24
Short name:
CA
p6-pol
Short name:
p6*
Alternative name(s):
PR
Retropepsin
Alternative name(s):
Exoribonuclease H (EC:3.1.13.2)
p66 RT
Integrase (EC:2.7.7.-By similarity, EC:3.1.-.-By similarity)
Short name:
IN
Gene namesi
Name:gag-pol
OrganismiSimian immunodeficiency virus agm.vervet (isolate AGM155) (SIV-agm.ver) (Simian immunodeficiency virus African green monkey vervet)
Taxonomic identifieri11727 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiCercopithecidae (Old World monkeys) [TaxID: 9527]

Subcellular locationi

Matrix protein p17 :
  • Virion Curated
  • Host nucleus By similarity
  • Host cytoplasm By similarity
  • Host cell membrane Curated; Lipid-anchor Curated
  • Note: Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane (By similarity).By similarity
Integrase :

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host membrane, Host nucleus, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00003059852 – 1470Gag-Pol polyproteinAdd BLAST1469
ChainiPRO_00003059862 – 141Matrix protein p17By similarityAdd BLAST140
ChainiPRO_0000305987142 – 372Capsid protein p24By similarityAdd BLAST231
ChainiPRO_0000305988373 – 439Nucleocapsid protein p7By similarityAdd BLAST67
ChainiPRO_0000305989440 – 511p6-polSequence analysisAdd BLAST72
ChainiPRO_0000305990512 – 612ProteaseBy similarityAdd BLAST101
ChainiPRO_0000305991613 – 1173Reverse transcriptase/ribonuclease HBy similarityAdd BLAST561
ChainiPRO_0000305992613 – 1053p51 RTBy similarityAdd BLAST441
ChainiPRO_00003059931054 – 1173p15By similarityAdd BLAST120
ChainiPRO_00003059941174 – 1470IntegraseBy similarityAdd BLAST297

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1

Post-translational modificationi

Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit.PROSITE-ProRule annotation
Capsid protein p24 is phosphorylated.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei141 – 142Cleavage; by viral proteaseBy similarity2
Sitei372 – 373Cleavage; by viral proteaseBy similarity2
Sitei439 – 440Cleavage; by viral proteaseBy similarity2
Sitei511 – 512Cleavage; by viral proteaseBy similarity2
Sitei612 – 613Cleavage; by viral proteaseSequence analysis2
Sitei1053 – 1054Cleavage; by viral proteaseBy similarity2
Sitei1173 – 1174Cleavage; by viral proteaseBy similarity2

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Matrix protein p17 is a trimer. Interacts with gp120. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. The integrase is a homodimer and possibly a homotetramer (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP27973.
SMRiP27973.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini531 – 602Peptidase A2PROSITE-ProRule annotationAdd BLAST72
Domaini658 – 848Reverse transcriptasePROSITE-ProRule annotationAdd BLAST191
Domaini1047 – 1170RNase HPROSITE-ProRule annotationAdd BLAST124
Domaini1227 – 1377Integrase catalyticPROSITE-ProRule annotationAdd BLAST151

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni841 – 849RT 'primer grip'By similarity9

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi16 – 22Nuclear export signalBy similarity7
Motifi26 – 32Nuclear localization signalBy similarity7
Motifi1011 – 1027Tryptophan repeat motifBy similarityAdd BLAST17

Domaini

The p66 RT is structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RNase H domain stabilizes the association of RT with primer-template (By similarity).By similarity
The tryptophan repeat motif is involved in RT p66/p51 dimerization.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri398 – 415CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri419 – 436CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1176 – 1217Integrase-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

CDDicd05482. HIV_retropepsin_like. 1 hit.
Gene3Di1.10.10.200. 1 hit.
1.10.1200.30. 1 hit.
1.10.375.10. 1 hit.
2.30.30.10. 1 hit.
2.40.70.10. 1 hit.
3.30.420.10. 2 hits.
4.10.60.10. 3 hits.
InterProiView protein in InterPro
IPR001969. Aspartic_peptidase_AS.
IPR000721. Gag_p24.
IPR017856. Integrase-like_N.
IPR036862. Integrase_C_dom_sf_retrovir.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR003308. Integrase_Zn-bd_dom_N.
IPR000071. Lentvrl_matrix_N.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom_sf.
IPR034170. Retropepsin-like_cat_dom.
IPR018061. Retropepsins.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix.
IPR012337. RNaseH-like_sf.
IPR002156. RNaseH_domain.
IPR036397. RNaseH_sf.
IPR000477. RT_dom.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
IPR001878. Znf_CCHC.
IPR036875. Znf_CCHC_sf.
PfamiView protein in Pfam
PF00540. Gag_p17. 1 hit.
PF00607. Gag_p24. 1 hit.
PF00552. IN_DBD_C. 1 hit.
PF02022. Integrase_Zn. 1 hit.
PF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF06815. RVT_connect. 1 hit.
PF06817. RVT_thumb. 1 hit.
PF00098. zf-CCHC. 2 hits.
PRINTSiPR00234. HIV1MATRIX.
SMARTiView protein in SMART
SM00343. ZnF_C2HC. 2 hits.
SUPFAMiSSF46919. SSF46919. 1 hit.
SSF47353. SSF47353. 1 hit.
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF50122. SSF50122. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 2 hits.
SSF57756. SSF57756. 1 hit.
PROSITEiView protein in PROSITE
PS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS51027. INTEGRASE_DBD. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
PS50158. ZF_CCHC. 2 hits.
PS50876. ZF_INTEGRASE. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

Note: Translation results in the formation of the Gag polyprotein most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.
Isoform Gag-Pol polyprotein (identifier: P27973-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGAATSALNR RQLDEFEHIR LRPNGKKKYQ IKHLIWAGKK MDRFGLHEKL
60 70 80 90 100
LETEEGCKKI IEVLSPLEPT GSEGMKSLYN LVCVLLCVHQ EKKVKDTEEA
110 120 130 140 150
LAIVRQCCHL VDKEKTAVTP PGGQQKNNTG GTATPGGSQN FPAQQQGNAW
160 170 180 190 200
VHVPLSPRTL NAWVKAVEEK KFGAEIVPMF QALSEGCTPY DINQMLNVLG
210 220 230 240 250
DHQGALQIVK EIINEEAAQW DVTHPPPAGP LPAGQLRDPG GSDIAGTTST
260 270 280 290 300
VQEQLEWIYT ANPRVDVGAI YRRWIILGLQ KCVKMYNPVS VLDIRQGPKE
310 320 330 340 350
PFKDYVDRFY KAIRAEQASG EVKQWMTESL LIQNANPDCK VILKGLGMHP
360 370 380 390 400
TLEEMLTACQ GVGGPSYKAK VMAEMMQNLQ SQNMVQQGGG RGRPRPPPKC
410 420 430 440 450
YNCGKFGHMQ RQCPEPRKIK CLKCGKPGHL AKDCRGQVNF FRVWPVDGDK
460 470 480 490 500
TKKFSRSHSW GGTKCAPSTE QLYTLRPSKE APAAVCRERE TNEKSEQKPP
510 520 530 540 550
SEQSRLERGI FFELPLWRRP IRTCIIGGTA VKALLDTGAD DTIIKDTDLQ
560 570 580 590 600
LRGSWRPKIV GGIGGGLNVK EYDNVEVQLE DKILRGTVLI GATPINIIGR
610 620 630 640 650
NFLAQAGAKL VMGQLSQTIP ITPVRLKEGA RGPRLKQWPL SKEKIIALQE
660 670 680 690 700
ICKTLEEEGK LSRVGGDNAY NTPVFCIRKK DKSQWRMLVD FRELNKATQD
710 720 730 740 750
FFEVQLGIPH PAGLKKMKQI TIIDVGDAYY SIPLDPEFRK YTAFTIPTVN
760 770 780 790 800
NEGPGIRYQF NCLPQGWKGS PTIFQNTASK ILEEIKKELK QLTIVQYMDD
810 820 830 840 850
LWVGSQEEGP KHDQLVQTLR NRLQEWGLET PEKKVQREPP FEWMGYKLWP
860 870 880 890 900
HKWKLQSIEL EKKEQWTVND LQKLVGKLNW AAQLYPGLRT KNICKLLRGK
910 920 930 940 950
KNLLDVVEWT PEAEAEYEEN KEILKTEQEG TYYAPEKPLR AAVQKLGDGQ
960 970 980 990 1000
WSYQFKQEGK ILKVGKFAKQ KATHTNELRV LAGVVQKIGK EALVIWGQLP
1010 1020 1030 1040 1050
TFELPVERDT WEQWWADYWQ VSWIPEWDFV SVPPLVTLWY TLTKEPIPGE
1060 1070 1080 1090 1100
DVYYVDGACN RQSKEGKAGY ITQQGKQRVQ QLENTTNQQA ELTAIKMALE
1110 1120 1130 1140 1150
DSGPKVNIVT DSQYAMGILT AQPTQSDSPL VEQIIAQMVQ KEAIYLQWVP
1160 1170 1180 1190 1200
AHKGIGGNEE IDKLVSKGVR RILFIGRIEE AQEEHDRYHS NWRNLADTFG
1210 1220 1230 1240 1250
LPQIVAKEIV AMCPKCQVKG EPIHGQVDAS PGVWQMDCTH IEGKIVIVAV
1260 1270 1280 1290 1300
HVASGFIEAE VIPRETGKET AKFLLKIIGR WPITHLHTDN GPNFTSQEVA
1310 1320 1330 1340 1350
AMCWWGKVEH TTGVPYNPQS QGSIESMNKQ LKEIIGKIRD DCQYTETAVL
1360 1370 1380 1390 1400
MACHIHNFKR KGGIGGLTAA ERLINMITTQ LEINTLQTKI QKILNFRVYY
1410 1420 1430 1440 1450
REGRDPVWKG PARLIWKGEG AVVLKEGEEL KVVPRRKAKI IKDYEPRKTL
1460 1470
GDETHLEGAG GSDHQMAGDS
Note: Produced by -1 ribosomal frameshifting.
Length:1,470
Mass (Da):165,744
Last modified:October 2, 2007 - v2
Checksum:iAAEE80A867552F17
GO
Isoform Gag polyprotein (identifier: P27972-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P27972.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.
Length:520
Mass (Da):57,735
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29975 Genomic RNA. Translation: AAA91906.1.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Similar proteinsi

Entry informationi

Entry nameiPOL_SIVV1
AccessioniPrimary (citable) accession number: P27973
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 2, 2007
Last modified: November 22, 2017
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme